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. 2004 May 10;165(3):347–356. doi: 10.1083/jcb.200310015

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Copyright © 2004, The Rockefeller University Press

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Figure 2. — Specific cleavage of caspase-4 by ER stress and Aβ treatment. (a) SK-N-SH cells were treated with 1 μg/ml tunicamycin (TM), 0.5 μM thapsigargin (TG), 100 μM etoposide (Etop), or 0.1 μM staurosporine (STS) for indicated periods, or irradiated with 150 J/m² UV followed by incubation for indicated periods. Equal amounts of cell lysates (15 μg) were analyzed by Western blotting using anti–caspase-4 antibody (top), anti–caspase-3 antibody (second from top), anti–caspase-7 antibody (third from top), or anti–β-actin antibody (bottom). Positions of pro–caspase-4, cleaved caspase-4, cleaved caspase-3, cleaved caspase-7, and β-actin are indicated. Extent of cell death assessed by MTS assay after incubation for indicated periods are also shown at the top of the gels. (b) SK-N-SH cells were treated with 25 μM synthetic Aβ_25-35 or 5 μM Aβ_1-40 peptides for the indicated periods. Equal amounts of cell lysates (15 μg) were analyzed by Western blotting using anti–caspase-4 antibody (top) and anti–β-actin antibody (bottom) as a control. Positions of pro–caspase-4, cleaved caspase-4, and β-actin are indicated. (c) SK-N-SH cells were treated with the reverse peptides (25 μM Aβ_35-25 and 5 μM Aβ_40-1, respectively) for the indicated periods, and cleavage of caspase-4 was examined as in panel b. (a–c) Bands marked by asterisks are likely to be derived from pro–caspase-4 by unknown processing reaction.